The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained , studies aimed at correlating structure and function, and experiments aimed at investigating protein folding. Structural studies for several proteins have been carried out. These include NfkB and Ref-a, complexes of human thioredoxin with its target site from DNA binding domains of Mu Transposase, the DNA binding domain of HIV-1 integrase, and the urea denatured state of Streptoccoccal Protein G. In addition, mutant core libraries of streptococcal Protein G have been prepared and characterized structurally as well as with respect to stability. Work is also carried out on a number of protein nucleic acid complexes, including those of GAGA, Are A and HMG-I/Y.